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GrainGenes Reference Report: BBA-1122-118

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Reference	BBA-1122-118
Title	Identification of a novel beta-turn-rich repeat motif in the d hordeins of barley
Journal	Biochimica et Biophysica Acta
Year	1992
Volume	1122
Pages	118-122
Author	Halford NG [ Show all 6 ]
Type	Article
Language	English
Abstract	The amino acid sequence of the C-terminal part of a barley D hordein seed protein was deduced from the nucleotide sequence of a partial cDNA. It showed high homology with the HMW glutenin subunits of wheat, both proteins consisting predominately of repeated sequences. Whereas the wheat repeats are based on tri-, hexa- and nonapeptides that are rich in glycine, proline and glutamine, the D hordein also contains eleven copies of a novel unrelated motif: Thr-Thr-Val-Ser. The repeated sequences in the wheat glutenin subunits have been demonstrated to form an unusual spiral supersecondary structure based on .beta.-turns. Conformational analysis of the Thr-Thr-Val- Ser motif by secondary structure prediction and by circular dichroism spectroscopy of an 18 residue synthetic peptide demonstrates that it also forms .beta.-turns. Thus, D hordein may also have a spiral structure like that of HMW glutenin, despite the presence of a different repeat motif. This conservation of protein conformation in D hordein and the wheat glutenin subunits may indicate a structural role, perhaps in packing of the proteins within the protein bodies of the developing grain.
Probe	pc257
Keyword	[ Hide all but 1 of 34 ] amino acid amino acid sequence barley base sequence biosynthesis cdna circular dichroism conformation conservation Deduced amino acid sequence DNA sequence genetics glutenin glutenin subunit glycine hmw glutenin homologies homology isolation and purification Molecular sequence data molecular sequence data nucleotide sequence peptide prediction protein conformation repeats repetitive sequence secondary secondary structure seed sequence spectroscopy Spiral Supersecondary structure

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